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Database: UniProt
Entry: A0A0J1J6G4_9FIRM
LinkDB: A0A0J1J6G4_9FIRM
Original site: A0A0J1J6G4_9FIRM 
ID   A0A0J1J6G4_9FIRM        Unreviewed;       284 AA.
AC   A0A0J1J6G4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=4Fe-4S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51379};
GN   ORFNames=RHS_1428 {ECO:0000313|EMBL:KLU72731.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU72731.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU72731.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU72731.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
CC   -!- SIMILARITY: Belongs to the nitroreductase family.
CC       {ECO:0000256|ARBA:ARBA00007118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLU72731.1}.
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DR   EMBL; JNGB01000013; KLU72731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1J6G4; -.
DR   PATRIC; fig|1504536.3.peg.993; -.
DR   Proteomes; UP000036477; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR029479; Nitroreductase.
DR   InterPro; IPR000415; Nitroreductase-like.
DR   PANTHER; PTHR43673; NAD(P)H NITROREDUCTASE YDGI-RELATED; 1.
DR   PANTHER; PTHR43673:SF10; PROTEIN DRGA; 1.
DR   Pfam; PF13237; Fer4_10; 1.
DR   Pfam; PF00881; Nitroreductase; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036477}.
FT   DOMAIN          21..50
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          58..78
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   284 AA;  32029 MW;  01D9D1403BAFAA83 CRC64;
     MNPVLAVSNP DYEEQAQSGG IMVVFDKELC TGCGACIKDC PGKAIKLAED KAQSCRPCIQ
     CGHCVAICPV NAVSIPEYEM DEVEEYVEAD FKVCPDHYLH ALKFRRSIRD FKEQKIERDK
     LDRILDAGRY TATAKNMQAC TFVLVQEQME EFRELLWNEI PGVLEILKES APDYERAFRS
     FYKKWQRNPK DDTFLFNAPA FLVIASQNPL DGGLAAANIE NMAVAEGAGA LYSGYMMRVL
     GTSPALQEWL GIGEKKVSCC MLLGYPNVKY RRTAPRRKAD VIWR
//
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